title: Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster.
abstract: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 Å resolution and belonged to space group P212121, with unit-cell parameters a=76.638, b=101.921, c=122.457 Å, α=β=γ=90°. Sequence alignment and structural analysis identified DmSCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl-CoA:acetate CoA transferase, DmSCOT has a different substrate-binding pocket, which may explain the difference in their substrate specificities.
authors.affiliation: School of Life Science, Anhui University, Hefei 230026, People's Republic of China.
authors.forename: Min
authors.initials: M
authors.lastname: Zhang
authors.forename: Han-Yang
authors.initials: HY
authors.lastname: Xu
authors.forename: Yi-Cui
authors.initials: YC
authors.lastname: Wang
authors.forename: Zhu-Bing
authors.initials: ZB
authors.lastname: Shi
authors.forename: Nan-Nan
authors.initials: NN
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D015256:Coenzyme A-Transferases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004331:Drosophila melanogaster / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013379:Substrate Specificity
chemical_list: D015256:Coenzyme A-Transferases; C021460:3-ketoacid CoA-transferase
keywords: Drosophila melanogaster; class I CoA transferases; succinyl-CoA:3-ketoacid CoA transferase